The use of affinity matrices in the purification of inhibin from bovine follicular fluid.
The protein associated with inhibin-like activity in bovine follicular fluid was purified 80- to 120-fold after successive adsorptions on different affinity matrices, i.e. Matrex gel red A, phenyl sepharose, omega-aminohexyl agarose and concanavalin-A sepharose. Partial characterization of the active protein resulted in the conclusion that inhibin from bovine follicular fluid is a hydrophobic glycoprotein with an apparent molecular weight between 60 000 and 70 000 daltons. An antiserum, raised against an 80-fold purified preparation, prevented the inhibin-like action of bovine follicular fluid on pituitary cells in vitro.
D000818:Animals; D002417:Cattle; D005260:Female; D005640:Follicle Stimulating Hormone / Q000378:metabolism; D007987:Gonadotropin-Releasing Hormone / Q000037:antagonists & inhibitors* / Q000494:pharmacology; D007265:Inhibins; D007986:Luteinizing Hormone / Q000378:metabolism; D008970:Molecular Weight; D006080:Ovarian Follicle / Q000032:analysis*; D010902:Pituitary Gland / Q000187:drug effects; D011506:Proteins / Q000302:isolation & purification* / Q000494:pharmacology; D013735:Testicular Hormones / Q000302:isolation & purification* / Q000494:pharmacology
D011506:Proteins; D013735:Testicular Hormones; D007987:Gonadotropin-Releasing Hormone; D007265:Inhibins; D007986:Luteinizing Hormone; D005640:Follicle Stimulating Hormone